Abstract:
:The present paper reports a modified method for isolation of lysostaphin--a bacteriolytic agent with specific affinity for staphylococcal cell wall. The proposed purification scheme includes three steps. The first procedure is ultrafiltration through a membrane filter giving a yield of 75.6%. The result of ultrafiltration is a concentrated, 10-times purified preparation of lysostaphin with specific activity 0.62 U/mg which can be used for digestion of S. aureus cells. Further step, performed by ion-exchange chromatography on DEAE-cellulose, yields a 60-times purified preparation containing a mixture of enzyme components of lysostaphin. The yield of this step is 47.2%, the preparation contains 3.54 U/mg protein. Using gel filtration on Sephadex G-50 a component with hexosaminidase activity was separated from the endopeptidase component on the basis of molar mass difference. A 270-times purified preparation of lysostaphin-endopeptidase with minimum of contaminating substances was obtained in this step. The yield of gel filtration was 22.1%, specific activity increased up to 16.3 U/mg protein.
journal_name
Folia Microbiol (Praha)journal_title
Folia microbiologicaauthors
Márová I,Dadák Vdoi
10.1007/BF02814386subject
Has Abstractpub_date
1993-01-01 00:00:00pages
245-52issue
3eissn
0015-5632issn
1874-9356journal_volume
38pub_type
杂志文章abstract::Biological activity of secondary metabolites produced by a plant-growth-promoting Pseudomonas fluorescens was evaluated. The strain produced antibiotics phenazine (PHE), 2,4-diacetylphloroglucinol (PHL) and siderophore pyoverdin (PYO) in standard King's B and succinic acid media, respectively. After extraction, PYO wa...
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